Publication

Pyridomycin bridges the NADH- and substratebinding pockets of the enoyl reductase InhA

Stewart Cole, Florence Pojer, Ruben Hartkoorn, Joao Pedro De Almeida Neres
2014
Journal Articles

Abstract

Pyridomycin, a natural product with potent antituberculosis activity, inhibits a major drug target, the InhA enoyl reductase. Here, we unveil the co-crystal structure and unique ability of pyridomycin to block both the NADH cofactor- and lipid substrate-binding pockets of InhA. This is to our knowledge a first-of-a-kind binding mode that discloses a new means of InhA inhibition. Proof-of-principle studies show how structure-assisted drug design can improve the activity of new pyridomycin derivatives.

Official source

https://infoscience.epfl.ch/entities/publication/116e2da3-d63f-4416-8b31-5826b8259c8b

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Pyridomycin bridges the NADH- and substratebinding pockets of the enoyl reductase InhA

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